{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T18:18:12Z","timestamp":1791397092401,"version":"4.3.3"},"reference-count":48,"publisher":"American Society for Microbiology","issue":"2","license":[{"start":{"date-parts":[[2010,1,15]],"date-time":"2010-01-15T00:00:00Z","timestamp":1263513600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["J Virol"],"published-print":{"date-parts":[[2010,1,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Mokola virus (MOKV) is a nonsegmented, negative-sense RNA virus that belongs to the\n            <jats:italic>Lyssavirus<\/jats:italic>\n            genus and\n            <jats:italic>Rhabdoviridae<\/jats:italic>\n            family. MOKV phosphoprotein P is an essential component of the replication and transcription complex and acts as a cofactor for the viral RNA-dependent RNA polymerase. P recruits the viral polymerase to the nucleoprotein-bound viral RNA (N-RNA) via an interaction between its C-terminal domain and the N-RNA complex. Here we present a structure for this domain of MOKV P, obtained by expression of full-length P in\n            <jats:italic>Escherichia coli<\/jats:italic>\n            , which was subsequently truncated during crystallization. The structure has a high degree of homology with P of rabies virus, another member of\n            <jats:italic>Lyssavirus<\/jats:italic>\n            genus, and to a lesser degree with P of vesicular stomatitis virus (VSV), a member of the related\n            <jats:italic>Vesiculovirus<\/jats:italic>\n            genus. In addition, analysis of the crystal packing of this domain reveals a potential binding site for the nucleoprotein N. Using both site-directed mutagenesis and yeast two-hybrid experiments to measure P-N interaction, we have determined the relative roles of key amino acids involved in this interaction to map the region of P that binds N. This analysis also reveals a structural relationship between the N-RNA binding domain of the P proteins of the\n            <jats:italic>Rhabdoviridae<\/jats:italic>\n            and the\n            <jats:italic>Paramyxoviridae<\/jats:italic>\n            .\n          <\/jats:p>","DOI":"10.1128\/jvi.01520-09","type":"journal-article","created":{"date-parts":[[2009,11,12]],"date-time":"2009-11-12T03:17:27Z","timestamp":1257995847000},"page":"1089-1096","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":31,"title":["Structure of the Nucleoprotein Binding Domain of Mokola Virus Phosphoprotein"],"prefix":"10.1128","volume":"84","author":[{"given":"Rene\u0301","family":"Assenberg","sequence":"first","affiliation":[{"name":"Division of Structural Biology and Oxford Protein Production Facility, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Olivier","family":"Delmas","sequence":"additional","affiliation":[{"name":"UPRE Lyssavirus Dynamics and Host Adaptation, WHO Collaborating Centre for Reference and Research on Rabies, Institut Pasteur, 75724 Paris Cedex 15, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jingshan","family":"Ren","sequence":"additional","affiliation":[{"name":"Division of Structural Biology and Oxford Protein Production Facility, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pierre-Olivier","family":"Vidalain","sequence":"additional","affiliation":[{"name":"Laboratoire de Ge\u0301nomique Virale et Vaccination, CNRS URA 3015, Institut Pasteur, 28 rue du Dr. Roux, 75724 Paris Cedex 15, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anil","family":"Verma","sequence":"additional","affiliation":[{"name":"Division of Structural Biology and Oxford Protein Production Facility, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Florence","family":"Larrous","sequence":"additional","affiliation":[{"name":"UPRE Lyssavirus Dynamics and Host Adaptation, WHO Collaborating Centre for Reference and Research on Rabies, Institut Pasteur, 75724 Paris Cedex 15, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Stephen C.","family":"Graham","sequence":"additional","affiliation":[{"name":"Division of Structural Biology and Oxford Protein Production Facility, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Fre\u0301de\u0301ric","family":"Tangy","sequence":"additional","affiliation":[{"name":"Laboratoire de Ge\u0301nomique Virale et Vaccination, CNRS URA 3015, Institut Pasteur, 28 rue du Dr. Roux, 75724 Paris Cedex 15, France"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jonathan M.","family":"Grimes","sequence":"additional","affiliation":[{"name":"Division of Structural Biology and Oxford Protein Production Facility, Wellcome Trust Centre for Human Genetics, University of Oxford, Roosevelt Drive, Oxford OX3 7BN, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Herve\u0301","family":"Bourhy","sequence":"additional","affiliation":[{"name":"UPRE Lyssavirus Dynamics and Host Adaptation, WHO Collaborating Centre for Reference and Research on Rabies, Institut Pasteur, 75724 Paris Cedex 15, 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